{"resolution": "1.0", "ligand_mw": "", "secondary_structure": "AADTWE#CEEECC&AADTWE#CEEECC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "", "remarks": "AMYLOID FORMING PEPTIDE AADTWE FROM TRANSTHYRETIN WITH ATTR-D38A MUTATION ASSOCIATED WITH A FAMILIAL FORM OF TRANSTHYRETIN AMYLOIDOSIS", "description": "They study amyloidogenic segments of transthyretin (TTR). TTR is a transporter of thyroxine and retinol in the blood and cerebrospinal fluid. When mutated and/or as a result of aging, TTR aggregates into amyloid fibrils that accumulate in organs such as the heart. The segments from the C-terminal region of TTR form in-register steric-zippers with highly-interdigitated, wet interfaces, whereas the Beta-strand B from the N-terminal region of TTR forms an out-of-register assembly, previously associated with oligomeric formation.", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "ALA-ALA-ASP-THR-TRP-GLU", "ligstr": "", "pmid": "29626847", "mutation_s_field": "D38A", "author": "Saelices, L., Sievers, S.A., Sawaya, M.R., Eisenberg, D.S.", "pdb_id": "6C3T", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.124", "protein_name": "Transthyretin", "gene_names": "", "global_stoichiometry": "Homo 20-mer - A20 ", "alternative_name": "", "peptide_protein_sequence": "chain-ID A: AADTWE; chain-ID B: AADTWE", "pdb_classification": "PROTEIN FIBRIL", "reference": "Protein Sci. 2018 Jul;27(7):1295-1303.", "length": "6", "entry": "S-0512"}